Significance of interactions of low molecular weight crystallin fragments in lens aging and cataract formation (Journal of Biological Chemistry (2008) 283, (8477-8485))

UV-C light promotes the reductive cleavage of disulfide bonds in β-Lactoglobulin and improves in vitro gastric digestion.

Freshly harvested Boletus edulis mushrooms are subjected to rapid loss of quality due to the high moisture content and enzymatic activity. Drying time, quality characteristics, microstructural and thermal properties were studied in mushrooms ground to puree subjected to hot air drying (HAD), freeze drying (FD) and centrifugal vacuum drying (CVD). The influence of hot water blanching and UV-C pretreatments was additionally investigated. The rehydration ability of mushroom powders was improved by FD, especially without pretreatment or combined to UV-C exposure. The HAD and CVD, with no pretreatment or combined to UV-C, ensured good preservation of phenolics and antioxidant activity of dried mushrooms. The total difference in color of mushroom pigments extracted in acetone was lower in samples dried by CVD and higher in ones by FD. Blanching before HAD produced whiter product probably due to the reduced polyphenoloxidase activity. Scanning Electron Microscopy (SEM) analysis showed fewer physical changes in FD-samples. Heat-induced structural changes were noticed by Differential Scanning Calorimetry (DSC), Thermogravimetry (TG) and Derivative Thermogravimetry (DTG) analysis, in particular of biopolymers, confirmed by ATR-FTIR analysis. Based on our complex approach, the UV pretreatment of mushrooms could be a better alternative to water blanching. Centrifugal vacuum emerged as a new efficient drying method in terms of bioactive compounds, color and thermal stability, while FD led to better rehydration ability and microstructure.

/pdf/influence-of-convective-and-vacuum-type-drying-on-quality-jp0anaxs.pdf

Influence of Convective and Vacuum-Type Drying on Quality, Microstructural, Antioxidant and Thermal Properties of Pretreated Boletus edulis Mushrooms

A new lectin from the floral capitula of Egletes viscosa (EgviL): Biochemical and biophysical characterization and cytotoxicity to human cancer cells.

A Novel Mutation (f71l) in aA-Crystallin Associated With Age-Related Cataract Results in Defective Chaperone-Like Function Despite Unaltered Structure

The conformation of lens protein α crystallin was investigated using different spectroscopic techniques under normal and UV-C-irradiated condition. The structural elucidation of commercially available lens protein α crystallin under the effects of UV-C irradiation has never been reported earlier. To study the effects of irradiation on the lens protein, we used UV–visible spectroscopy, CD spectroscopy, and steady-state and time-resolved fluorescence measurements along with FTIR study, under increasing doses of UV-C irradiation. Using the secondary and tertiary structural changes as parameters for detecting conformational perturbation, we investigated the structural paradigm shift in the lens protein α crystallin. Increasing doses of UV-C radiation resulted in decreasing β sheet content of α crystallin from 30 to 10%. The fluorescence profile confirmed the formation of ROS species in the protein upon extensive exposure to UV-C irradiation. These results inferred UV-C irradiation may induce alteration of secondary structure of the lens protein leading to impaired biological functioning.

Aberration in the structural paradigm of lens protein α crystallin by UV-C irradiation

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Aberration in the structural paradigm of lens protein α crystallin by UV-C irradiation